Research workbench
X-ray structure of furin in complex with the cyclic peptide C[GLUTARYL-arg-arg-lys]-arg-4-amba
Analyse X-ray structure of furin in complex with the cyclic peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HZA
- Type
- protein
- Length
- 477 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Furin; Arg-arg-lys-arg-00S
- EC
- 3.4.21.75
- UniProt
- P09958
- Ligands
- 00S, PTD, CA, NA, PO4, CL
- Pockets
- 5 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Furin (EC 3.4.21.75) | protein | 473 | 21% helix, 28% strand | P09958 |
| B | Arg-arg-lys-arg-00S | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- 00S · 4-(aminomethyl)benzenecarboximidamide · ligand · chains A, B
- PTD · Pentanedial · ligand · chains A, B
- CA · Calcium ion · metal · 3 copies · chains A
- NA · Sodium ion · metal · 3 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.46 | 0.78 | 15 | empty |
| 2 | 52 | 0.33 | 0.78 | 12 | empty |
| 3 | 79 | 0.32 | 0.75 | 27 | empty |
| 4 | 57 | 0.26 | 0.73 | 13 | empty |
| 5 | 50 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 475 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent, 3 disulfide (covalent ligand, disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09958
- Elsewhere: RCSB PDB 6HZA · PDBe 6HZA · UniProt P09958
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